Inactivation of Enzymes in Fresh Sake Using a Continuous Flow System for High-Pressure Carbonation
The Inactivation kinetics of α-glucosidase, glucoamylase, α-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure ca...
Gespeichert in:
| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2005, Vol.69 (11), p.2094-2100 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2100 |
|---|---|
| container_issue | 11 |
| container_start_page | 2094 |
| container_title | Bioscience, biotechnology, and biochemistry |
| container_volume | 69 |
| creator | TANIMOTO, Shota MATSUMOTO, Hideyuki FUJII, Kazuyoshi OHDOI, Ritsushi SAKAMOTO, Koji IZUWA, Shinya YAMANE, Yuichi MIYAKE, Masaki SHIMODA, Mitsuya OSAJIMA, Yutaka |
| description | The Inactivation kinetics of α-glucosidase, glucoamylase, α-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure carbonated sake were investigated. Among the enzymes investigated, α-glucosidase was the most stable and α-amylase was the most labile on inactivation under carbonation. The decimal reduction times (D values) of α-glucosidase, glucoamylase, α-amylase (extrapolated from the Z value), and acid carboxypeptidase were 29, 6, 2, and 5 min respectively at 45 °C. These values are lower than those subjected to heat treatment. On the carbonation treatment as well as the heat treatment, ethanol accelerated the inactivation of all four enzymes, but glucose depressed the inactivation of these enzymes, except for acid carboxypeptidase. These results suggest that this continuous flow system enabled effective inactivation of enzymes in fresh sake. |
| doi_str_mv | 10.1271/bbb.69.2094 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1791886137</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>68827596</sourcerecordid><originalsourceid>FETCH-LOGICAL-c648t-5bce43b1ccb3beba7e460fc257a39bd6531c8742efd4c012eee8983ea5144ff43</originalsourceid><addsrcrecordid>eNqF0V1rFDEUBuAgil2rV95LQJSCzJpMvi9l6dpCQaH2OiTZpE2dSWoyY1l_vWl3S0FErwKH57yc8ALwGqMl7gX-aK1dcrXskaJPwAITKjquqHgKFkhh3knK8AF4Ues1Qm3A8HNwgDlBnCu0APY0GTfFn2aKOcEc4HH6tR19hTHBdfH1Cp6b7x5e1JguoYGrnKaY5jxXuB7yLTzf1smPMOQCT-LlVfe1rdS5eLgyxeZ0n_oSPAtmqP7V_j0EF-vjb6uT7uzL59PVp7POcSqnjlnnKbHYOUust0Z4ylFwPROGKLvhjGAnBe192FCHcO-9l0oSbximNARKDsH7Xe5NyT9mXyc9xur8MJjk28GaS9kLpniDR_-EWCgsJcdE_DcT3wci1eDbP-B1nktq_9XtPCUxYoI19WGnXMm1Fh_0TYmjKVuNkb4rU7cyNVf6rsym3-wzZzv6zaPdt9fAuz0w1ZkhFJNcrI9OUMkYI83xnYupNTWa21yGjZ7MdsjlYYn87YLf-5W5OQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1449810575</pqid></control><display><type>article</type><title>Inactivation of Enzymes in Fresh Sake Using a Continuous Flow System for High-Pressure Carbonation</title><source>J-STAGE Free</source><source>MEDLINE</source><source>Oxford University Press Journals All Titles (1996-Current)</source><source>Freely Accessible Japanese Titles</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>TANIMOTO, Shota ; MATSUMOTO, Hideyuki ; FUJII, Kazuyoshi ; OHDOI, Ritsushi ; SAKAMOTO, Koji ; IZUWA, Shinya ; YAMANE, Yuichi ; MIYAKE, Masaki ; SHIMODA, Mitsuya ; OSAJIMA, Yutaka</creator><creatorcontrib>TANIMOTO, Shota ; MATSUMOTO, Hideyuki ; FUJII, Kazuyoshi ; OHDOI, Ritsushi ; SAKAMOTO, Koji ; IZUWA, Shinya ; YAMANE, Yuichi ; MIYAKE, Masaki ; SHIMODA, Mitsuya ; OSAJIMA, Yutaka</creatorcontrib><description>The Inactivation kinetics of α-glucosidase, glucoamylase, α-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure carbonated sake were investigated. Among the enzymes investigated, α-glucosidase was the most stable and α-amylase was the most labile on inactivation under carbonation. The decimal reduction times (D values) of α-glucosidase, glucoamylase, α-amylase (extrapolated from the Z value), and acid carboxypeptidase were 29, 6, 2, and 5 min respectively at 45 °C. These values are lower than those subjected to heat treatment. On the carbonation treatment as well as the heat treatment, ethanol accelerated the inactivation of all four enzymes, but glucose depressed the inactivation of these enzymes, except for acid carboxypeptidase. These results suggest that this continuous flow system enabled effective inactivation of enzymes in fresh sake.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.69.2094</identifier><identifier>PMID: 16306690</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Alcoholic Beverages ; alpha-Amylases - metabolism ; alpha-Glucosidases - metabolism ; Bacteria - cytology ; Bacteria - enzymology ; Biological and medical sciences ; Carbohydrates - pharmacology ; Carbonates - pharmacology ; Carboxypeptidase C ; Cathepsin A - metabolism ; Enzyme Stability ; Enzymes ; Ethanol ; Ethanol - pharmacology ; fresh sake ; Fundamental and applied biological sciences. Psychology ; Glucan 1,4-alpha-Glucosidase - metabolism ; Glucoamylase ; Glucose ; Heat treatments ; high-pressure carbonation ; inactivation kinetics of enzymes ; Kinetics ; Microbial Viability ; Pressure ; Q1 ; Sake ; Sugar</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2005, Vol.69 (11), p.2094-2100</ispartof><rights>2005 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2005</rights><rights>2006 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c648t-5bce43b1ccb3beba7e460fc257a39bd6531c8742efd4c012eee8983ea5144ff43</citedby><cites>FETCH-LOGICAL-c648t-5bce43b1ccb3beba7e460fc257a39bd6531c8742efd4c012eee8983ea5144ff43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,4010,27904,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17485553$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16306690$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>TANIMOTO, Shota</creatorcontrib><creatorcontrib>MATSUMOTO, Hideyuki</creatorcontrib><creatorcontrib>FUJII, Kazuyoshi</creatorcontrib><creatorcontrib>OHDOI, Ritsushi</creatorcontrib><creatorcontrib>SAKAMOTO, Koji</creatorcontrib><creatorcontrib>IZUWA, Shinya</creatorcontrib><creatorcontrib>YAMANE, Yuichi</creatorcontrib><creatorcontrib>MIYAKE, Masaki</creatorcontrib><creatorcontrib>SHIMODA, Mitsuya</creatorcontrib><creatorcontrib>OSAJIMA, Yutaka</creatorcontrib><title>Inactivation of Enzymes in Fresh Sake Using a Continuous Flow System for High-Pressure Carbonation</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>The Inactivation kinetics of α-glucosidase, glucoamylase, α-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure carbonated sake were investigated. Among the enzymes investigated, α-glucosidase was the most stable and α-amylase was the most labile on inactivation under carbonation. The decimal reduction times (D values) of α-glucosidase, glucoamylase, α-amylase (extrapolated from the Z value), and acid carboxypeptidase were 29, 6, 2, and 5 min respectively at 45 °C. These values are lower than those subjected to heat treatment. On the carbonation treatment as well as the heat treatment, ethanol accelerated the inactivation of all four enzymes, but glucose depressed the inactivation of these enzymes, except for acid carboxypeptidase. These results suggest that this continuous flow system enabled effective inactivation of enzymes in fresh sake.</description><subject>Alcoholic Beverages</subject><subject>alpha-Amylases - metabolism</subject><subject>alpha-Glucosidases - metabolism</subject><subject>Bacteria - cytology</subject><subject>Bacteria - enzymology</subject><subject>Biological and medical sciences</subject><subject>Carbohydrates - pharmacology</subject><subject>Carbonates - pharmacology</subject><subject>Carboxypeptidase C</subject><subject>Cathepsin A - metabolism</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Ethanol</subject><subject>Ethanol - pharmacology</subject><subject>fresh sake</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucan 1,4-alpha-Glucosidase - metabolism</subject><subject>Glucoamylase</subject><subject>Glucose</subject><subject>Heat treatments</subject><subject>high-pressure carbonation</subject><subject>inactivation kinetics of enzymes</subject><subject>Kinetics</subject><subject>Microbial Viability</subject><subject>Pressure</subject><subject>Q1</subject><subject>Sake</subject><subject>Sugar</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0V1rFDEUBuAgil2rV95LQJSCzJpMvi9l6dpCQaH2OiTZpE2dSWoyY1l_vWl3S0FErwKH57yc8ALwGqMl7gX-aK1dcrXskaJPwAITKjquqHgKFkhh3knK8AF4Ues1Qm3A8HNwgDlBnCu0APY0GTfFn2aKOcEc4HH6tR19hTHBdfH1Cp6b7x5e1JguoYGrnKaY5jxXuB7yLTzf1smPMOQCT-LlVfe1rdS5eLgyxeZ0n_oSPAtmqP7V_j0EF-vjb6uT7uzL59PVp7POcSqnjlnnKbHYOUust0Z4ylFwPROGKLvhjGAnBe192FCHcO-9l0oSbximNARKDsH7Xe5NyT9mXyc9xur8MJjk28GaS9kLpniDR_-EWCgsJcdE_DcT3wci1eDbP-B1nktq_9XtPCUxYoI19WGnXMm1Fh_0TYmjKVuNkb4rU7cyNVf6rsym3-wzZzv6zaPdt9fAuz0w1ZkhFJNcrI9OUMkYI83xnYupNTWa21yGjZ7MdsjlYYn87YLf-5W5OQ</recordid><startdate>2005</startdate><enddate>2005</enddate><creator>TANIMOTO, Shota</creator><creator>MATSUMOTO, Hideyuki</creator><creator>FUJII, Kazuyoshi</creator><creator>OHDOI, Ritsushi</creator><creator>SAKAMOTO, Koji</creator><creator>IZUWA, Shinya</creator><creator>YAMANE, Yuichi</creator><creator>MIYAKE, Masaki</creator><creator>SHIMODA, Mitsuya</creator><creator>OSAJIMA, Yutaka</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>2005</creationdate><title>Inactivation of Enzymes in Fresh Sake Using a Continuous Flow System for High-Pressure Carbonation</title><author>TANIMOTO, Shota ; MATSUMOTO, Hideyuki ; FUJII, Kazuyoshi ; OHDOI, Ritsushi ; SAKAMOTO, Koji ; IZUWA, Shinya ; YAMANE, Yuichi ; MIYAKE, Masaki ; SHIMODA, Mitsuya ; OSAJIMA, Yutaka</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c648t-5bce43b1ccb3beba7e460fc257a39bd6531c8742efd4c012eee8983ea5144ff43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Alcoholic Beverages</topic><topic>alpha-Amylases - metabolism</topic><topic>alpha-Glucosidases - metabolism</topic><topic>Bacteria - cytology</topic><topic>Bacteria - enzymology</topic><topic>Biological and medical sciences</topic><topic>Carbohydrates - pharmacology</topic><topic>Carbonates - pharmacology</topic><topic>Carboxypeptidase C</topic><topic>Cathepsin A - metabolism</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Ethanol</topic><topic>Ethanol - pharmacology</topic><topic>fresh sake</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucan 1,4-alpha-Glucosidase - metabolism</topic><topic>Glucoamylase</topic><topic>Glucose</topic><topic>Heat treatments</topic><topic>high-pressure carbonation</topic><topic>inactivation kinetics of enzymes</topic><topic>Kinetics</topic><topic>Microbial Viability</topic><topic>Pressure</topic><topic>Q1</topic><topic>Sake</topic><topic>Sugar</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TANIMOTO, Shota</creatorcontrib><creatorcontrib>MATSUMOTO, Hideyuki</creatorcontrib><creatorcontrib>FUJII, Kazuyoshi</creatorcontrib><creatorcontrib>OHDOI, Ritsushi</creatorcontrib><creatorcontrib>SAKAMOTO, Koji</creatorcontrib><creatorcontrib>IZUWA, Shinya</creatorcontrib><creatorcontrib>YAMANE, Yuichi</creatorcontrib><creatorcontrib>MIYAKE, Masaki</creatorcontrib><creatorcontrib>SHIMODA, Mitsuya</creatorcontrib><creatorcontrib>OSAJIMA, Yutaka</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>TANIMOTO, Shota</au><au>MATSUMOTO, Hideyuki</au><au>FUJII, Kazuyoshi</au><au>OHDOI, Ritsushi</au><au>SAKAMOTO, Koji</au><au>IZUWA, Shinya</au><au>YAMANE, Yuichi</au><au>MIYAKE, Masaki</au><au>SHIMODA, Mitsuya</au><au>OSAJIMA, Yutaka</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inactivation of Enzymes in Fresh Sake Using a Continuous Flow System for High-Pressure Carbonation</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2005</date><risdate>2005</risdate><volume>69</volume><issue>11</issue><spage>2094</spage><epage>2100</epage><pages>2094-2100</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>The Inactivation kinetics of α-glucosidase, glucoamylase, α-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure carbonated sake were investigated. Among the enzymes investigated, α-glucosidase was the most stable and α-amylase was the most labile on inactivation under carbonation. The decimal reduction times (D values) of α-glucosidase, glucoamylase, α-amylase (extrapolated from the Z value), and acid carboxypeptidase were 29, 6, 2, and 5 min respectively at 45 °C. These values are lower than those subjected to heat treatment. On the carbonation treatment as well as the heat treatment, ethanol accelerated the inactivation of all four enzymes, but glucose depressed the inactivation of these enzymes, except for acid carboxypeptidase. These results suggest that this continuous flow system enabled effective inactivation of enzymes in fresh sake.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>16306690</pmid><doi>10.1271/bbb.69.2094</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2005, Vol.69 (11), p.2094-2100 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1791886137 |
| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Alcoholic Beverages alpha-Amylases - metabolism alpha-Glucosidases - metabolism Bacteria - cytology Bacteria - enzymology Biological and medical sciences Carbohydrates - pharmacology Carbonates - pharmacology Carboxypeptidase C Cathepsin A - metabolism Enzyme Stability Enzymes Ethanol Ethanol - pharmacology fresh sake Fundamental and applied biological sciences. Psychology Glucan 1,4-alpha-Glucosidase - metabolism Glucoamylase Glucose Heat treatments high-pressure carbonation inactivation kinetics of enzymes Kinetics Microbial Viability Pressure Q1 Sake Sugar |
| title | Inactivation of Enzymes in Fresh Sake Using a Continuous Flow System for High-Pressure Carbonation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T23%3A21%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Inactivation%20of%20Enzymes%20in%20Fresh%20Sake%20Using%20a%20Continuous%20Flow%20System%20for%20High-Pressure%20Carbonation&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=TANIMOTO,%20Shota&rft.date=2005&rft.volume=69&rft.issue=11&rft.spage=2094&rft.epage=2100&rft.pages=2094-2100&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/10.1271/bbb.69.2094&rft_dat=%3Cproquest_cross%3E68827596%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1449810575&rft_id=info:pmid/16306690&rfr_iscdi=true |